|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
125-380 |
1.81e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 125 WHYRRSYTAIQNDSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELET 204
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 205 CHHQLDSTRHELSLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQ 284
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 285 ELIAAQNLCTELKSALSGKEGDLVAVNAELTELHKLNESLSADLNKVTLVSQGYEAEVAEQSNELKTLQAKVMKLEATLE 364
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250
....*....|....*.
gi 1717564029 365 AEKTISESLKGTIDTL 380
Cdd:COG1196 474 LLEAALAELLEELAEA 489
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
136-352 |
2.23e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 136 NDSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHE 215
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 216 LSLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNaglsrqcDQLSQTVSDTKAERDRFEQELIAAQNLCTE 295
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL-------EELSEELRELESKRSELRRELEELREKLAQ 926
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717564029 296 LKSALSGKEGDLVAVNAELTELHKLN-ESLSADLNKVTLVSQGYEAEVAEQSNELKTL 352
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQERLSEEYSLTlEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
137-355 |
7.13e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 7.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 137 DSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHEL 216
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 217 SLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCTEL 296
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717564029 297 KSALSGKEGDLVAVNAELTELHKLNESLSADLNKVTLVSQGYEAEVAEQSNELKTLQAK 355
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
135-372 |
9.72e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 135 QNDSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETchhqldstrh 214
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 215 elslAQQSNDSLSQQLAERKTEIAGHLEYQKKLNE----EINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQ 290
Cdd:COG4942 88 ----LEKEIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 291 NLCTELKSALSGKEGDLVAVNAELTELHKLNESLSADLNKVTLVSQGYEAEVAEQSNELKTLQAKVMKLEATLEAEKTIS 370
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 1717564029 371 ES 372
Cdd:COG4942 244 PA 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-369 |
6.11e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 149 LEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQQSNDSLSQ 228
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 229 QLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQnlCTELKSALSGKEGDLV 308
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELE 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717564029 309 AVNAELtelhklnESLSADLNKVTLVSQGYEAEVAEQSNELKTLQAKVMKLEATLEAEKTI 369
Cdd:TIGR02168 458 RLEEAL-------EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
138-361 |
1.83e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 138 SVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELS 217
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 218 LAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCTELK 297
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717564029 298 SALSGKEGDLVAVNAELTELHKLNESLSADLNKvtLVSQGYEAEVAEQSNELKTLQAKVMKLEA 361
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAE--AAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
133-360 |
2.30e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 133 AIQNDSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQalqgRLEIRDSTVKELETRLNVAEAELETCHHQLDST 212
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA----RLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 213 RHELSLAQQSNDSLSQQLAERkteiaghleyQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNL 292
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQ----------IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717564029 293 CTELKSALSGKEGDLVAVNAELTELHKLNESLSADLNKVTLVSQGYEAEVAEQSNELKTLQAKVMKLE 360
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-380 |
2.46e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 149 LEEEVTQLLQRLEQSAtdmdELKLENQALQGRLEIRDstvkeletrLNVAEAELETCHHQLDSTRHELSLAQQSNDSLSQ 228
Cdd:COG1196 194 ILGELERQLEPLERQA----EKAERYRELKEELKELE---------AELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 229 QLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCTELKSALSGKEGDLV 308
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717564029 309 AVNAELTELHKLNESLSADLNKVTLVSQGYEAEVAEQSNELKTLQAKVMKLEATLEAEKTISESLKGTIDTL 380
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
137-380 |
9.90e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 137 DSVKKAEARSMQLEEEVTQLLQRLEqsatDMDELKLENQALQGRLeiRDSTVKELETRLNVAEAELETCHHQLDSTRHEL 216
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLR----REREKAERYQALLKEK--REYEGYELLKEKEALERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 217 slaqqsnDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNA-GLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCTE 295
Cdd:TIGR02169 254 -------EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 296 LKSALSGKEGDLVAVNAELTELHKLNESLSADLNKVTLVSQGYEAEVAEQSNELKTLQAKVMKLEATLEAEKTISESLKG 375
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
....*
gi 1717564029 376 TIDTL 380
Cdd:TIGR02169 407 ELDRL 411
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
135-370 |
1.93e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 135 QNDSVKKAEARSMQ--LEEEVTQLLQRLEQSATDMDELKLENQ--ALQGRLEIRDSTVKELETRLNVAEAELETchhqld 210
Cdd:COG3206 164 QNLELRREEARKALefLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAE------ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 211 strhelslAQQSNDSLSQQLAERKTEIAGHLEyqkklNEEINTQRSDNAGLSRQCDQLSQTVSDT-------KAERDRFE 283
Cdd:COG3206 238 --------AEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNhpdvialRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 284 QELIAaqnlctELKSALSGKEGDLVAVNAELTELHKLNESLSADLNKVTLVSQGY-----EAEVAEQSneLKTLQAKVMk 358
Cdd:COG3206 305 AQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELrrlerEVEVAREL--YESLLQRLE- 375
|
250
....*....|..
gi 1717564029 359 lEATLEAEKTIS 370
Cdd:COG3206 376 -EARLAEALTVG 386
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-374 |
2.06e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 104 RYLDIPDEVKVALGDIiSYITWHYRRSYTAIQNDSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEI 183
Cdd:TIGR02168 214 RYKELKAELRELELAL-LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 184 RDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQQSNDSLSQQLAERKTEIAG---------------HLEYQ---- 244
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeelesleaeleelEAELEeles 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 245 --KKLNEEINTQRSDNAGLSRQCDQ-------LSQTVSDTKAERDRFEQELIAAQNLCTELKsaLSGKEGDLVAVNAELT 315
Cdd:TIGR02168 373 rlEELEEQLETLRSKVAQLELQIASlnneierLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELE 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717564029 316 ELHKLNESLSADLNKVTLVSQGYEAEVAEQSNELKTLQAKVMKLEATLEAEKTISESLK 374
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
138-366 |
7.69e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 138 SVKKAEARSMQLEEEVTQLLQRLEQSATDMDEL-------KLENQALQGRLEIRDSTVKELETRLNVAEAELEtcHHQLD 210
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLeqeienvKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIP 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 211 STRHELSLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQ 290
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717564029 291 NLCTELKSALSGKEGDLVAVNAELTELHKLNESLSADLNKVTLVSQGYEAEVAEQSNELKTLQAKVMKLEATLEAE 366
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
126-290 |
8.44e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 126 HYRRSYTAIQNDSVKKAEArsmqLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAeletc 205
Cdd:COG4913 596 RRIRSRYVLGFDNRAKLAA----LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA----- 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 206 HHQLDSTRHELSLAQQSND---SLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRF 282
Cdd:COG4913 667 EREIAELEAELERLDASSDdlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
....*...
gi 1717564029 283 EQELIAAQ 290
Cdd:COG4913 747 LRALLEER 754
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
177-380 |
2.10e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 177 LQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRS 256
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 257 DNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCTELKSALSGKEGDLVAVNAE---------------------LT 315
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerleslerriaaterrLE 841
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717564029 316 ELHKLNESLSADLNKVTLVSQGYEAEVAEQSNELKTLQAKVMKLEATLEAEKTISESLKGTIDTL 380
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
141-304 |
3.60e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 141 KAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQ 220
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 221 QSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCTELKSAL 300
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
....
gi 1717564029 301 SGKE 304
Cdd:TIGR02169 493 AEAE 496
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
142-288 |
1.76e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 142 AEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQQ 221
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717564029 222 SNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIA 288
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
137-376 |
2.29e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 137 DSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELK-------------LENQALQGRLEIRDSTVKELETRLNVAEAELE 203
Cdd:PRK11281 73 DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKddndeetretlstLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 204 TCHHQLDSTRHELSLAQQSNDSLSQQLAERKTE-IAGHLEYQKKLNEE---INTQ----RSDNAGLSRQCDQLSQTVSDT 275
Cdd:PRK11281 153 SLQTQPERAQAALYANSQRLQQIRNLLKGGKVGgKALRPSQRVLLQAEqalLNAQndlqRKSLEGNTQLQDLLQKQRDYL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 276 KAERDRFEQELIAAQNLCTELKSALSGKEGDlVAVNAELTELHKLNESLSADLNKVTLVSQgYEAEVAEQSNEL--KTLQ 353
Cdd:PRK11281 233 TARIQRLEHQLQLLQEAINSKRLTLSEKTVQ-EAQSQDEAARIQANPLVAQELEINLQLSQ-RLLKATEKLNTLtqQNLR 310
|
250 260
....*....|....*....|....*.
gi 1717564029 354 AKvMKLEATLEAEKTISE---SLKGT 376
Cdd:PRK11281 311 VK-NWLDRLTQSERNIKEqisVLKGS 335
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
213-380 |
2.44e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 213 RHELSLAQQSNDSLSQQLAErkteiaghleyqkkLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFeqeliaaQNL 292
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAE--------------LADLLSLERQGNQDLQDSVANLRASLSAAEAERSRL-------QAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 293 CTELKSALSGKEGDLVAVNAELTELHKLNESlsaDLNKVTLVSQGYEAevaeqsnelktLQAKVMKLEATLEAEKTISES 372
Cdd:PRK09039 104 LAELAGAGAAAEGRAGELAQELDSEKQVSAR---ALAQVELLNQQIAA-----------LRRQLAALEAALDASEKRDRE 169
|
....*...
gi 1717564029 373 LKGTIDTL 380
Cdd:PRK09039 170 SQAKIADL 177
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
138-362 |
3.14e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 138 SVKKAEARSMQLEEEVTQLLQRlEQSATDMDEL-KLENQALQGRLEIRDSTvkeletrlNVAEAELETCHHQLDSTRHEL 216
Cdd:pfam15921 288 SSARSQANSIQSQLEIIQEQAR-NQNSMYMRQLsDLESTVSQLRSELREAK--------RMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 217 SLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDN-------AGLSRQCDQLSQTVSDTKAERDRFEQELIAA 289
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNkrlwdrdTGNSITIDHLRRELDDRNMEVQRLEALLKAM 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717564029 290 QNLCT----ELKSALSGKEGDLVAVNAELTELHKLNESLSADLNKVTLVSQGYEAEVAEQSNELKTLQAKVMKLEAT 362
Cdd:pfam15921 439 KSECQgqmeRQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT 515
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
137-354 |
3.63e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 137 DSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHEL 216
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 217 SLAQQSNDSLSQQL-AERKTEIAGHLEYQKKL----NEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQN 291
Cdd:COG3883 96 YRSGGSVSYLDVLLgSESFSDFLDRLSALSKIadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717564029 292 LCTELKSALSGKEGDLVAVNAELTELHKLNESLSADLNKVTLVSQGYEAEVAEQSNELKTLQA 354
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
149-307 |
3.86e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 149 LEEEVTQLLQRLEQSATDMDELkleNQAL----QGRLEIRDStVKELETRLNVAEAELETCHHQLDSTRHELSLAQQSND 224
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAEL---ADLLslerQGNQDLQDS-VANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 225 SLSQQLAERKTEIAGHLEYQKKLNEEIntqrsdnAGLSRQCDQLsQTVSDTKAERDRFEQELIAAqnLCTELKSALSGKE 304
Cdd:PRK09039 120 ELAQELDSEKQVSARALAQVELLNQQI-------AALRRQLAAL-EAALDASEKRDRESQAKIAD--LGRRLNVALAQRV 189
|
...
gi 1717564029 305 GDL 307
Cdd:PRK09039 190 QEL 192
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
140-306 |
3.99e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.90 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 140 KKAEARSMQLEEEVTQLLQRLEQSATDM---DELKLEN------QALQGrlEIRDSTV--KELETRLNV----------- 197
Cdd:NF012221 1565 ERAEADRQRLEQEKQQQLAAISGSQSQLestDQNALETngqaqrDAILE--ESRAVTKelTTLAQGLDAldsqatyages 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 198 --------AEAELETCHHQLDSTRH----ELSLAQQSNDSLSQQL--AERKTEIAGHLEYQKKLNEEINTQRSDNAGLSR 263
Cdd:NF012221 1643 gdqwrnpfAGGLLDRVQEQLDDAKKisgkQLADAKQRHVDNQQKVkdAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKR 1722
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1717564029 264 QCDQLSQTVSDTKAERD----------RFEQELIAAQNLCTELKSALSG---KEGD 306
Cdd:NF012221 1723 KDDALAKQNEAQQAESDanaaandaqsRGEQDASAAENKANQAQADAKGakqDESD 1778
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
139-345 |
4.86e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 139 VKKAEARSMQLEEEVTQLLQRLEQS-ATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAEletcHHQLDSTRHELS 217
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNQLlRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQ----HGAFLDADIETA 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 218 LAQQSN-DSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSdnAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCTEL 296
Cdd:pfam12128 343 AADQEQlPSWQSELENLEERLKALTGKHQDVTAKYNRRRS--KIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQAL 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1717564029 297 KSALSGKegdLVAVNAELTELHKLNESLSADLnKVTLVSQGYEAEVAEQ 345
Cdd:pfam12128 421 ESELREQ---LEAGKLEFNEEEYRLKSRLGEL-KLRLNQATATPELLLQ 465
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
180-366 |
4.99e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 180 RLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSdna 259
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 260 glSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCTELKSALSGKEGDLVAVNAELTELHKlneslsadlnkvtlvsqGYE 339
Cdd:COG1579 88 --NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA-----------------ELD 148
|
170 180
....*....|....*....|....*..
gi 1717564029 340 AEVAEQSNELKTLQAKVMKLEATLEAE 366
Cdd:COG1579 149 EELAELEAELEELEAEREELAAKIPPE 175
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
180-364 |
7.24e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 180 RLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQQSndslsQQLAERKTEIAGHLEYQKKLNEEINTQRSDNA 259
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL-----AEYSWDEIDVASAEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 260 GLsrqcDQLSQTVSDTKAERDRFEQELIAAQNLCTELKSALSGKEGDLVAVNAELTELHKLNES-LSADLNKV--TLVSQ 336
Cdd:COG4913 686 DL----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERfaAALGD 761
|
170 180
....*....|....*....|....*....
gi 1717564029 337 GYEAEVAEQ-SNELKTLQAKVMKLEATLE 364
Cdd:COG4913 762 AVERELRENlEERIDALRARLNRAEEELE 790
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
128-317 |
8.39e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 128 RRSYTAIQNDSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELEtchh 207
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR---- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 208 QLDSTRHElSLAQQSnDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRsdnAGLSRQCDQLSQTVSDTKAERDRFEQELi 287
Cdd:COG4913 334 GNGGDRLE-QLEREI-ERLERELEERERRRARLEALLAALGLPLPASA---EEFAALRAEAAALLEALEEELEALEEAL- 407
|
170 180 190
....*....|....*....|....*....|
gi 1717564029 288 aaqnlcTELKSALSGKEGDLVAVNAELTEL 317
Cdd:COG4913 408 ------AEAEAALRDLRRELRELEAEIASL 431
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
134-373 |
9.00e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 134 IQNDSVKKAEARSMQLEEEVtQLLQRLE-----------QSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAE- 201
Cdd:PLN02939 115 QQTNSKDGEQLSDFQLEDLV-GMIQNAEknilllnqarlQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEk 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 202 --LETCHHQLDSTRHELSlaqqsndslsqqlaerkTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAEr 279
Cdd:PLN02939 194 ihVEILEEQLEKLRNELL-----------------IRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAET- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 280 drfEQELIAAQNLCTELKSALSGKEGDLVAVNAELTELHKLN--------ESLSADLNKVTLVSQGYeAEVAEQSNELKT 351
Cdd:PLN02939 256 ---EERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQydcwwekvENLQDLLDRATNQVEKA-ALVLDQNQDLRD 331
|
250 260
....*....|....*....|..
gi 1717564029 352 lqaKVMKLEATLEAEKTISESL 373
Cdd:PLN02939 332 ---KVDKLEASLKEANVSKFSS 350
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
148-394 |
1.05e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 148 QLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQQSNDSLS 227
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 228 QQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCTELKSALSGKEGDL 307
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 308 VAVNAELTELHKLNESLSADLNKVTLVSQGYEAEVAEQSNELKTLQAKVMKLEATLEAEKTISESLKGTIDTLTGAMAGG 387
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
....*..
gi 1717564029 388 GTGKSKQ 394
Cdd:COG4372 275 EEELEIA 281
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
135-292 |
3.95e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 135 QNDSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRH 214
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717564029 215 ELSLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNL 292
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
142-365 |
4.69e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.17 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 142 AEARSMQLEEEVTQLLQR---LE---QSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHE 215
Cdd:COG3096 304 EQYRLVEMARELEELSAResdLEqdyQAASDHLNLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEAR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 216 LSLAQQSNDSLSQQLAERKTEI-AGH---LEYQKKLNEEINTQR--------SDNAG-----LSRQCDQLSQTV------ 272
Cdd:COG3096 384 LEAAEEEVDSLKSQLADYQQALdVQQtraIQYQQAVQALEKARAlcglpdltPENAEdylaaFRAKEQQATEEVleleqk 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 273 -SDTKAERDRFEQELIAAQNLCTELKSALSGKE---------------GDLVAVNAELTELHKLNES------LSADLNK 330
Cdd:COG3096 464 lSVADAARRQFEKAYELVCKIAGEVERSQAWQTarellrryrsqqalaQRLQQLRAQLAELEQRLRQqqnaerLLEEFCQ 543
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1717564029 331 -----------VTLVSQGYEAEVAEQSNELKTLQAKVMKLEATLEA 365
Cdd:COG3096 544 rigqqldaaeeLEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
142-264 |
8.28e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.36 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 142 AEARSMQLEEEVTQL---LQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSL 218
Cdd:COG4913 659 DEIDVASAEREIAELeaeLERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1717564029 219 AQQSNDS-LSQQLAERKTEIAG---HLEYQKKLNEEINTQRSDNAGLSRQ 264
Cdd:COG4913 739 AEDLARLeLRALLEERFAAALGdavERELRENLEERIDALRARLNRAEEE 788
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
137-232 |
9.14e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 37.95 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717564029 137 DSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDS-------TVKELETRLNVA---EAELETCH 206
Cdd:pfam07888 157 ERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTqvlqlqdTITTLTQKLTTAhrkEAENEALL 236
|
90 100
....*....|....*....|....*.
gi 1717564029 207 HQLDSTRHELSLAQQSNDSLSQQLAE 232
Cdd:pfam07888 237 EELRSLQERLNASERKVEGLGEELSS 262
|
|
| |
